Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action.
Autor: | Hématy K; Department of Plant Molecular Biology, University of Lausanne, Lausanne 1015, Switzerland.; Institut Jean-Pierre Bourgin, INRAe, AgroParisTech, Université Paris-Saclay, 78000 Versailles, France., De Bellis D; Department of Plant Molecular Biology, University of Lausanne, Lausanne 1015, Switzerland.; Electron Microscopy Facility, University of Lausanne, Lausanne 1015, Switzerland., Wang X; Institute of Biotechnology, HiLIFE, University of Helsinki, Helsinki 00014, Finland.; Faculty of Biological and Environmental Sciences and Viikki Plant Science Centre, Organismal and Evolutionary Biology Research Programme, University of Helsinki, Helsinki 00014, Finland., Mähönen AP; Institute of Biotechnology, HiLIFE, University of Helsinki, Helsinki 00014, Finland.; Faculty of Biological and Environmental Sciences and Viikki Plant Science Centre, Organismal and Evolutionary Biology Research Programme, University of Helsinki, Helsinki 00014, Finland., Geldner N; Department of Plant Molecular Biology, University of Lausanne, Lausanne 1015, Switzerland. |
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Jazyk: | angličtina |
Zdroj: | Plant physiology [Plant Physiol] 2022 Jun 01; Vol. 189 (2), pp. 557-566. |
DOI: | 10.1093/plphys/kiac019 |
Abstrakt: | The exocyst is the main plasma membrane vesicle-tethering complex in eukaryotes and is composed of eight different subunits. Yet, in plant genomes, many subunits display multiple copies, thought to reflect evolution of complex subtypes with divergent functions. In Arabidopsis thaliana root endodermal cells, the isoform EXO70A1 is required for positioning of CASP1 at the Casparian Strip Domain, but not for its non-targeted secretion to the plasma membrane. Here, we show that exo84b resembles exo70a1 mutants regarding CASP1 mistargeting and secretion of apoplastic proteins, but exo84b additionally affects secretion of other integral plasma membrane proteins. Moreover, conditional, cell-type-specific gene editing of the single-copy core component SEC6 allows visualization of secretion defects in plant cells with a complete lack of exocyst complex function. Our approach opens avenues for deciphering the complexity/diversity of exocyst functions in plant cells and enables analysis of central trafficking components with lethal phenotypes. (© The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists.) |
Databáze: | MEDLINE |
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